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The length of time that a voltage-dependent channel stays open can have a profound impact on the functional consequences of its opening. Together, Ca2+ and the Ca2+-binding protein calmodulin regulate the closing (Ca2+-dependent inactivation) and facilitate the opening (Ca2+-dependent facilitation) of voltage-gated Ca2+ channels. This review describes the features of calmodulin and its binding sites on voltage-gated Ca2+ channels that are likely to contribute to its ability to drive these opposing effects on channel activity.
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